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M213222200v1
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Papers In Press, published online ahead of print April 7, 2003
J. Biol. Chem, 10.1074/jbc.M213222200
Submitted on December 27, 2002
Revised on March 24, 2003
Accepted on April 7, 2003

ICA69 is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells

Folker Spitzenberger, Susan Pietropaolo, Paul Verkade, Bianca Habermann, Sandra Lacas-Gervais, Hassan Mziaut, Massimo Pietropaolo, and Michele Solimena

Experimental Diabetology, University of Technology - Dresden, Dresden 01307

Corresponding Author: michele.solimena{at}mailbox.tu-dresden.de

Islet Cell Autoantigen (ICA) 69 is a cytosolic protein of still unknown function. Involvement of ICA69 in neurosecretion has been suggested by the impairment of acetylcholine release at neuromuscular junctions upon mutation of its homologue gene ric-19 in C. Elegans. In this study we have further investigated the localization of ICA69 in neurons and insulinoma INS-1 cells. ICA69 was enriched in the perinuclear region, while it did not co-localize with markers of synaptic vesicles/synaptic-like microvesicles. Confocal microscopy and subcellular fractionation in INS-1 cells showed co-localization of ICA69 with markers of the Golgi complex and, to a minor extent, with immature insulin-containing secretory granules. The association of ICA69 with these organelles was confirmed by immunoelectronmicroscopy. Virtually no ICA69 immunogold labelling was observed on secretory granules near the plasma membrane, suggesting that ICA69 dissociates from secretory granule membranes during their maturation. In silico sequence and structural analyses revealed that the N-terminal region of ICA69 is similar to the region of Arfaptins that interacts with ARF1, a small GTP-ase involved in vesicle budding at the Golgi complex and immature secretory granules. ICA69 is therefore a novel Arfaptin-related protein which is likely to play a role in membrane trafficking at the Golgi complex and immature secretory granules in neurosecretory cells.


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